Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: possible involvement in obesity-linked insulin resistance.

By L. Khamzina, A. Veilleux, S. Bergeron, A. Marette. Endocrinology, 2005

594 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/6931b00a3e374e82992e65efebc07f0cb362b371

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

Citations in the corpus

Cardiac Metabolism and Its Interactions with Contraction, Growth, and Survival of the Cardiomyocte (2013, background): “This effect of fatty acids on mTOR has been previously shown in skeletal muscle and liver tissue of rats fed a high-fat diet.(189,190) In addition, incubation of myotubes with palmitate increased phosphorylation of S6 kinase, a downstream target of mTOR.”
mTOR Signaling in Growth, Metabolism, and Disease (2017, background): “…(left), and the consequences of chronic mTORC1 inhibition (middle) or ct of rapamycin or a theoretical mTORC1-specific inhibitor. muscle leads to atrophy, whereas optimal muscle growth and function requires Cell 168, March 9, 2017 967 acids, and pro-inflammatory cytokines (Khamzina et al., 2005).”
Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2 (2012, background): “Rodents fed a high-fat diet to cause obesity and insulin resistance show increased basal mTORC1→S6K activation in metabolic tissues, with pronounced phosphorylation of IRS1 at S632 and/or S302 (hS636, hS307) [106, 115].”
mTOR signaling in growth control and disease (2012, unknown): “The expansion of adipose tissue that characterizes the obese state represents the main risk factor for the development of insulin resistance and type 2 diabetes, and mTORC1 is highly active in the tissues of obese and high-fat-fed rodents (Khamzina et al., 2005; Tremblay et al., 2007; Um et al., 200”
Akt stimulates hepatic SREBP1c and lipogenesis through parallel mTORC1-dependent and independent pathways (2011, background): “Elevated levels of mTORC1 signaling have been associated with conditions of hepatic insulin resistance (Khamzina et al., 2005; Koketsu et al., 2008; Mordier and Iynedjian, 2007).”
mTOR Signaling in Growth, Metabolism, and Disease. (2017, background): “Indeed, obese or high fat diet (HFD) treated mice have high mTORC1 signaling in many tissues, including the pancreas, likely due to increased levels of circulating insulin, amino acids, and pro-inflammatory cytokines (Khamzina et al., 2005).”
Physiological frailty index (PFI): quantitative in-life estimate of individual biological age in mice (2017, unknown): “It has been previously demonstrated that in rodents HFD-induced obesity increases activation of mTOR pathway in liver and skeletal muscle [16].”
Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, unknown): “Interestingly, mTOR activity is increased in obesity (Khamzina et al., 2005), and this augmented signaling may play a role in abnormal insulin action associated with the obese state.”
Regulation of mTORC1 and its impact on gene expression at a glance (2013, background): “Obesity and nutrient overload, which are linked to NAFLD, exacerbate mTORC1 activity in the liver (Khamzina et al., 2005; Tremblay et al., 2007), which, in turn, might promote NAFLD by activating SREBP1.”
Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress (2010, background): “Many reports hypothesize that inhibition of mTORC1 contributes to the manifestation of these stress-related phenotypes (Khamzina et al., 2005; Kimball et al., 2000; Lang et al., 2010; McGhee et al., 2009).”
Autophagy and signaling: their role in cell survival and cell death (2005, background): “mTOR-downstream targets, evidence is now accumulating that the overactivation of mTOR leads to the inhibition of the proximal part of the insulin-signaling pathway.(56,57) This is because of phosphorylation of IRS1 by S6K, which results in decreased binding of the p85 regulatory subunit of PI3K to I”